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Ratnaparkhi, Girish S and Varadarajan, R (2001) Osmolytes stabilize Ribonuclease S by stabilizing its fragments S protein and S peptide to compact folding-competent states. In: Journal of Biological Chemistry, 276 (31). pp. 28789-28798.
Ratnaparkhi, Girish S and Varadarajan, R (2000) Thermodynamic and structural studies of cavity formation in proteins suggest that loss of packing interactions rather than the hydrophobic effect dominates the observed energetics. In: Biochemistry, 39 (40). pp. 12365-12374.
Ratnaparkhi, Girish S and Awasthi, Satish Kumar and Rani, P and Balaram, P and Varadarajan, R (2000) Structural and thermodynamic consequences of introducing alpha-aminoisobutyric acid in the S peptide of ribonuclease S. In: Protein Engineering, 13 (10). pp. 697-702.
Ratnaparkhi, Girish S and Varadarajan, R (2000) Thermodynamic and Structural Studies of Cavity Formation in Proteins Suggest That Loss of Packing Interactions Rather Than the Hydrophobic Effect Dominates the Observed Energetics. In: Biochemistry, 39 (40). pp. 12365-12374.
Ratnaparkhi, Girish S and Varadarajan, R (1999) X-ray Crystallographic Studies of the Denaturation of Ribonuclease S. In: Proteins:Structure, Function, and Genetics, 36 (3). pp. 282-294.
Ratnaparkhi, Girish S and Ramachandran, S and Udgaonkar, Jayant B and Varadarajan, R (1998) Discrepancies between the NMR and X-ray structures of uncomplexed barstar: Analysis suggests that packing densities of protein structures determined by NMR are unreliable. In: Biochemistry, 37 (19). pp. 6958-6966.
Ratnaparkhi, Girish S and Varadarajan, R (1997) Structural studies of protein unfolding. In: Current Science (Bangalore), 72 (11). pp. 826-830.
Nadig, Gautham and Ratnaparkhi, Girish S and Varadarajan, Raghavan and Vishveshwara, Saraswathi (1996) Dynamics of ribonuclease A and ribonuclease S: Computational and experimental studies. In: Protein Science, 05 (10). pp. 2104-2114.
Thomson, James and Ratnaparkhi, Girish S and Varadarajan, Raghavan and Sturtevant, Julian M and Richards, Frederic M (1994) Thermodynamic and structural consequences of changing a sulfur atom to a methylene group in the M13Nle mutation in ribonuclease-S. In: Biochemistry, 33 (28). pp. 8587-8593.
